English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
 Local TagsRelease HistoryDetailsSummary
  High-resolution NMR determination of the dynamic structure of membrane proteins.

Jaremko, M., Jaremko, L., Villinger, S., Schmidt, C. D., Griesinger, C., Becker, S., et al. (2016). High-resolution NMR determination of the dynamic structure of membrane proteins. Angewandte Chemie International Edition, 55(35), 101518-10521. doi:10.1002/anie.201602639.

Item is

 

show all hide all

Basic

show hide
Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-34DA-C Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-34E0-B
Genre: Journal Article

Files

show Files
hide Files
:
2337954.pdf (Publisher version), 5MB
 
File Permalink:
-
Name:
2337954.pdf
Description:
-
OA-Status:
Visibility:
Restricted (UNKNOWN id 303; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2337954_Suppl.pdf (Supplementary material), 4MB
View   Save
File Permalink:
https://hdl.handle.net/11858/00-001M-0000-002B-34DD-6
Name:
2337954_Suppl.pdf
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
View
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Jaremko, M.1, Author           
Jaremko, L.1, Author           
Villinger, S.1, Author           
Schmidt, C. D.2, Author           
Griesinger, C.2, Author           
Becker, S.2, Author           
Zweckstetter, M.1, Author           
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

Content

show
hide
Free keywords: NMR spectroscopy; membrane proteins; protein dynamics; relaxation; structure determination
 Abstract: (15) N spin-relaxation rates are demonstrated to provide critical information about the long-range structure and internal motions of membrane proteins. Combined with an improved calculation method, the relaxation-rate-derived structure of the 283-residue human voltage-dependent anion channel revealed an anisotropically shaped barrel with a rigidly attached N-terminal helix. Our study thus establishes an NMR spectroscopic approach to determine the structure and dynamics of mammalian membrane proteins at high accuracy and resolution.

Details

show
hide
Language(s): eng - English
 Dates: 2016-07-272016-08-22
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/anie.201602639
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Angewandte Chemie International Edition
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 55 (35) Sequence Number: - Start / End Page: 101518 - 10521 Identifier: -